Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay.

Virology - 20 Feb 2012

Chang Kyeong-Ok, Takahashi Daisuke, Prakash Om, Kim Yunjeong

Abstract excerpt

Noroviruses are the major cause of food- or water-borne gastroenteritis outbreaks in humans. The norovirus protease that cleaves a large viral polyprotein to nonstructural proteins is essential for virus replication and an attractive target for antiviral drug development. Noroviruses show high genetic diversity with at least five genogroups, GI-GV, of which GI and GII are responsible for the majority of norovirus...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Down-Regulation
Share to Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Gastroenteritis

Share to Norovirus

Share to Oligopeptides

Share to Peptide Hydrolases

Share to Protease Inhibitors

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22200497
DOI: 10.1016/j.virol.2011.12.002
PMCID: PMC3259199

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay.PMID 22200497Read ↗

Development of a Gaussia Luciferase-Based Human Norovirus Protease Reporter System: Cell Type-Specific Profile of Norwalk Virus Protease Precursors and Evaluation of InhibitorsSemantic proximity Read ↗

Essential Role of Enterovirus 2A Protease in Counteracting Stress Granule Formation and the Induction of Type I InterferonSemantic proximity Read ↗

Norovirus Protease Structure and Antivirals Development.Semantic proximity Read ↗

A Novel Class of Norovirus Inhibitors Targeting the Viral Protease with Potent Antiviral Activity In Vitro and In Vivo.Semantic proximity Read ↗

Crystal Structure of Inhibitor-Bound GII.4 Sydney 2012 Norovirus 3C-Like Protease.Semantic proximity Read ↗

Conformational flexibility is a critical factor in designing broad-spectrum human norovirus protease inhibitorsSemantic proximity Read ↗

Establishment of a green fluorescent protein (GFP)-based reporter for picornaviral 3C proteasesSemantic proximity Read ↗

Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enterovirusesSemantic proximity Read ↗

Elucidating the Implications of Norovirus N- and O-Glycosylation, O-GlcNAcylation, and Phosphorylation.Semantic proximity Read ↗

Selective human enterovirus and rhinovirus inhibitors: An overview of capsid‐binding and protease‐inhibiting moleculesSemantic proximity Read ↗

Mutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activitiesSemantic proximity Read ↗

Norovirus: targets and tools in antiviral drug discovery.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.